Cysteine transaminase

In enzymology, a cysteine transaminase (EC 2.6.1.3) is an enzyme that catalyzes the chemical reaction

L-cysteine + 2-oxoglutarate mercaptopyruvate + L-glutamate
cysteine transaminase
Identifiers
EC no.2.6.1.3
CAS no.9030-32-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Thus, the two substrates of this enzyme are L-cysteine and 2-oxoglutarate, whereas its two products are mercaptopyruvate and L-glutamate.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-cysteine:2-oxoglutarate aminotransferase. Other names in common use include cysteine aminotransferase, L-cysteine aminotransferase, and CGT. This enzyme participates in cysteine metabolism. It employs one cofactor, pyridoxal phosphate.

References

    • CHATAGNER F, SAURET-IGNAZI G (June 1956). "[Role of transamination and pyridoxal phosphate in the enzymatic formation of hydrogen sulfide from cysteine by the rat liver under anaerobiosis.]". Bull. Soc. Chim. Biol. Paris. 38 (2–3): 415–28. PMID 13342749.


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